Metal ions as cofactors for the binding of inhibitors to methionine aminopeptidase: A critical view of the relevance of in vitro metalloenzyme assays
- 31 December 2004
- journal article
- research article
- Published by Wiley
- Vol. 44 (23) , 3620-3623
- https://doi.org/10.1002/anie.200500592
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Likelihood-enhanced fast rotation functionsActa Crystallographica Section D-Biological Crystallography, 2004
- Crystal Structures of Staphylococcus aureus Methionine Aminopeptidase Complexed with Keto Heterocycle and Aminoketone Inhibitors Reveal the Formation of a Tetrahedral IntermediateJournal of Medicinal Chemistry, 2004
- Protonation States of Methionine Aminopeptidase and Their Relevance for Inhibitor Binding and Catalytic ActivityPublished by Elsevier ,2003
- Discovery and Structural Modification of Inhibitors of Methionine Aminopeptidases from Escherichia coli and Saccharomyces cerevisiaeJournal of Medicinal Chemistry, 2003
- Extreme Zinc-Binding Thermodynamics of the Metal Sensor/Regulator Protein, ZntRJournal of the American Chemical Society, 2001
- Escherichia coliMethionine Aminopeptidase: Implications of Crystallographic Analyses of the Native, Mutant, and Inhibited Enzymes for the Mechanism of Catalysis,Biochemistry, 1999
- Structure of Human Methionine Aminopeptidase-2 Complexed with FumagillinScience, 1998
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- PROCHECK: a program to check the stereochemical quality of protein structuresJournal of Applied Crystallography, 1993
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991